PDBe 1nsg

X-ray diffraction
2.2Å resolution

THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP

Released:
Source organism: Homo sapiens
Primary publication:
Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 55 736-44 (1999)
PMID: 10089303

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase FKBP1A Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Best match: P62942 (Residues: 2-108)
Gene names: FKBP1, FKBP12, FKBP1A
Serine/threonine-protein kinase mTOR Chain: B
Molecule details ›
Chain: B
Length: 94 amino acids
Theoretical weight: 11.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Best match: P42345 (Residues: 2019-2112)
Gene names: FRAP, FRAP1, FRAP2, MTOR, RAFT1, RAPT1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 46.3Å b: 52.4Å c: 102Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.265
Expression system: Escherichia coli